ID   LUXU_VIBCH              Reviewed;         113 AA.
AC   Q9KT83;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Phosphorelay protein LuxU;
GN   Name=luxU; OrderedLocusNames=VC_1022;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
RN   [2]
RP   FUNCTION.
RX   PubMed=12176318; DOI=10.1016/s0092-8674(02)00829-2;
RA   Miller M.B., Skorupski K., Lenz D.H., Taylor R.K., Bassler B.L.;
RT   "Parallel quorum sensing systems converge to regulate virulence in Vibrio
RT   cholerae.";
RL   Cell 110:303-314(2002).
RN   [3]
RP   AUTOINDUCER 2 (AI-2) SYNTHESIS IN V.CHOLERAE.
RX   PubMed=9190823; DOI=10.1128/jb.179.12.4043-4045.1997;
RA   Bassler B.L., Greenberg E.P., Stevens A.M.;
RT   "Cross-species induction of luminescence in the quorum-sensing bacterium
RT   Vibrio harveyi.";
RL   J. Bacteriol. 179:4043-4045(1997).
CC   -!- FUNCTION: Phosphorelay protein which receives sensory signals from a
CC       sensory kinase and transmit them to LuxO. At low cell density, a
CC       phosphoryl group is transferred from the sensory kinase, probably on
CC       His-57 and this phosphoryl group is further transferred to LuxO.
CC       {ECO:0000269|PubMed:12176318}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
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DR   EMBL; AE003852; AAF94181.1; -; Genomic_DNA.
DR   PIR; D82250; D82250.
DR   RefSeq; NP_230667.1; NC_002505.1.
DR   RefSeq; WP_001209531.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KT83; -.
DR   SMR; Q9KT83; -.
DR   STRING; 243277.VC_1022; -.
DR   PRIDE; Q9KT83; -.
DR   DNASU; 2614292; -.
DR   EnsemblBacteria; AAF94181; AAF94181; VC_1022.
DR   GeneID; 57739705; -.
DR   GeneID; 66939757; -.
DR   KEGG; vch:VC_1022; -.
DR   PATRIC; fig|243277.26.peg.976; -.
DR   eggNOG; COG2198; Bacteria.
DR   HOGENOM; CLU_168256_0_0_6; -.
DR   OMA; TEMAYRE; -.
DR   BioCyc; VCHO:VC1022-MON; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0004672; F:protein kinase activity; IEA:UniProt.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.160; -; 1.
DR   InterPro; IPR036641; HPT_dom_sf.
DR   InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR   Pfam; PF01627; Hpt; 1.
DR   SUPFAM; SSF47226; SSF47226; 1.
DR   PROSITE; PS50894; HPT; 1.
PE   3: Inferred from homology;
KW   Phosphoprotein; Reference proteome; Two-component regulatory system.
FT   CHAIN           1..113
FT                   /note="Phosphorelay protein LuxU"
FT                   /id="PRO_0000220140"
FT   DOMAIN          18..113
FT                   /note="HPt"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00110"
FT   MOD_RES         57
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   113 AA;  12679 MW;  408848E66CF8883C CRC64;
     MREWINQSKI DLLAKEIGEE NVPILVNIFL GELNDYQSKL VSDTVADKLG YLKEISHALK
     SSAASFGADR LCAKAVELDS RAKSGEMMDI SLEVEHMLEL LKQTHQCYSD LVH